BPI_HUMAN
ID BPI_HUMAN Reviewed; 487 AA.
AC P17213; B2RCY2; Q1ZZU8; Q5JRW0; Q8IW58; Q9BYZ9; Q9H1L2; Q9H1M8; Q9H203;
AC Q9UCT4; Q9UD65;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Bactericidal permeability-increasing protein;
DE Short=BPI;
DE AltName: Full=CAP 57;
DE Flags: Precursor;
GN Name=BPI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-68, FUNCTION,
RP SUBCELLULAR LOCATION, DOMAIN, AND VARIANTS VAL-16 AND LYS-216.
RX PubMed=2722846; DOI=10.1016/s0021-9258(18)60560-5;
RA Gray P.W., Flaggs G., Leong S.R., Gumina R.J., Weiss J., Ooi C.E.,
RA Elsbach P.;
RT "Cloning of the cDNA of a human neutrophil bactericidal protein. Structural
RT and functional correlations.";
RL J. Biol. Chem. 264:9505-9509(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7517398; DOI=10.1016/s0021-9258(17)32454-7;
RA Wilde C.G., Seilhamer J.J., McGrogan M., Ashton N., Snable J.L., Lane J.C.,
RA Leong S.R., Thornton M.B., Miller K.L., Scott R.W.;
RT "Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-
RT binding protein. LPS binding properties and effects on LPS-mediated cell
RT activation.";
RL J. Biol. Chem. 269:17411-17416(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-16.
RA Ma H., Cao X., Sun Y., Lei W.;
RT "cDNA cloning and sequence analysis of human bactericidal/permeability
RT protein.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-404.
RC TISSUE=Fetal heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-216.
RC TISSUE=Leukocyte;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-487, AND VARIANTS LYS-216 AND ASP-404.
RA Xu J., Wang H.;
RT "Cloning of cDNA of human bactericidal/permeability-increasing protein.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 32-53, AND FUNCTION.
RC TISSUE=Leukocyte;
RX PubMed=1937776; DOI=10.1128/iai.59.11.4193-4200.1991;
RA Wasiluk K.R., Skubitz K.M., Gray B.H.;
RT "Comparison of granule proteins from human polymorphonuclear leukocytes
RT which are bactericidal toward Pseudomonas aeruginosa.";
RL Infect. Immun. 59:4193-4200(1991).
RN [9]
RP PROTEIN SEQUENCE OF 32-51.
RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N.,
RA Seeger M., Nathan C.F.;
RT "Antibiotic proteins of human polymorphonuclear leukocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
RN [10]
RP PROTEIN SEQUENCE OF 32-48.
RX PubMed=3667613; DOI=10.1016/s0021-9258(18)48110-0;
RA Ooi C.E., Weiss J., Elsbach P., Frangione B., Mannion B.;
RT "A 25-kDa NH2-terminal fragment carries all the antibacterial activities of
RT the human neutrophil 60-kDa bactericidal/permeability-increasing protein.";
RL J. Biol. Chem. 262:14891-14894(1987).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-49; CYS-163; CYS-166
RP AND CYS-206.
RX PubMed=8812832; DOI=10.1006/prep.1996.0071;
RA Horwitz A.H., Leigh S.D., Abrahamson S., Gazzano-Santoro H., Liu P.-S.,
RA Williams R.E., Carroll S.F., Theofan G.;
RT "Expression and characterization of cysteine-modified variants of an amino-
RT terminal fragment of bactericidal/permeability-increasing protein.";
RL Protein Expr. Purif. 8:28-40(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 32-487.
RX PubMed=9188532; DOI=10.1126/science.276.5320.1861;
RA Beamer L.J., Carroll S.F., Eisenberg D.;
RT "Crystal structure of human BPI and two bound phospholipids at 2.4-A
RT resolution.";
RL Science 276:1861-1864(1997).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 32-487, AND DISULFIDE BOND.
RX PubMed=10843855; DOI=10.1006/jmbi.2000.3805;
RA Kleiger G., Beamer L.J., Grothe R., Mallick P., Eisenberg D.;
RT "The 1.7 A crystal structure of BPI: a study of how two dissimilar amino
RT acid sequences can adopt the same fold.";
RL J. Mol. Biol. 299:1019-1034(2000).
CC -!- FUNCTION: The cytotoxic action of BPI is limited to many species of
CC Gram-negative bacteria; this specificity may be explained by a strong
CC affinity of the very basic N-terminal half for the negatively charged
CC lipopolysaccharides that are unique to the Gram-negative bacterial
CC outer envelope. Has antibacterial activity against the Gram-negative
CC bacterium P.aeruginosa, this activity is inhibited by LPS from
CC P.aeruginosa. {ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2722846}.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked.
CC {ECO:0000269|PubMed:8812832}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8812832}.
CC Cytoplasmic granule membrane {ECO:0000269|PubMed:2722846}.
CC Note=Membrane-associated in polymorphonuclear Leukocytes (PMN)
CC granules. {ECO:0000269|PubMed:2722846}.
CC -!- TISSUE SPECIFICITY: Restricted to cells of the myeloid series.
CC -!- DOMAIN: The N-terminal region may be exposed to the interior of the
CC granule, whereas the C-terminal portion may be embedded in the
CC membrane. During phagocytosis and degranulation, proteases may be
CC released and activated and cleave BPI at the junction of the N- and C-
CC terminal portions of the molecule, providing controlled release of the
CC N-terminal antibacterial fragment when bacteria are ingested.
CC {ECO:0000269|PubMed:2722846}.
CC -!- DOMAIN: The N- and C-terminal barrels adopt an identical fold despite
CC having only 13% of conserved residues. {ECO:0000269|PubMed:10843855}.
CC -!- SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.
CC {ECO:0000305}.
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DR EMBL; J04739; AAA51841.1; -; mRNA.
DR EMBL; DQ414688; ABD66755.1; -; mRNA.
DR EMBL; AK315328; BAG37729.1; -; mRNA.
DR EMBL; AL359555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL499625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040955; AAH40955.1; -; mRNA.
DR EMBL; AF322588; AAG42844.1; -; mRNA.
DR PIR; A33850; A30909.
DR RefSeq; NP_001716.2; NM_001725.2.
DR PDB; 1BP1; X-ray; 2.40 A; A=32-487.
DR PDB; 1EWF; X-ray; 1.70 A; A=32-487.
DR PDBsum; 1BP1; -.
DR PDBsum; 1EWF; -.
DR AlphaFoldDB; P17213; -.
DR SMR; P17213; -.
DR BioGRID; 107139; 14.
DR IntAct; P17213; 1.
DR STRING; 9606.ENSP00000262865; -.
DR DrugBank; DB04178; Di-Stearoyl-3-Sn-Phosphatidylcholine.
DR TCDB; 1.C.40.1.1; the bactericidal permeability increasing protein (bpip) family.
DR GlyGen; P17213; 1 site.
DR iPTMnet; P17213; -.
DR PhosphoSitePlus; P17213; -.
DR BioMuta; BPI; -.
DR DMDM; 215274242; -.
DR EPD; P17213; -.
DR jPOST; P17213; -.
DR MassIVE; P17213; -.
DR MaxQB; P17213; -.
DR PaxDb; P17213; -.
DR PeptideAtlas; P17213; -.
DR PRIDE; P17213; -.
DR ProteomicsDB; 53463; -.
DR Antibodypedia; 26835; 355 antibodies from 31 providers.
DR DNASU; 671; -.
DR Ensembl; ENST00000262865.9; ENSP00000262865.4; ENSG00000101425.14.
DR GeneID; 671; -.
DR KEGG; hsa:671; -.
DR UCSC; uc002xib.3; human.
DR CTD; 671; -.
DR DisGeNET; 671; -.
DR GeneCards; BPI; -.
DR HGNC; HGNC:1095; BPI.
DR HPA; ENSG00000101425; Tissue enriched (bone).
DR MIM; 109195; gene.
DR neXtProt; NX_P17213; -.
DR OpenTargets; ENSG00000101425; -.
DR PharmGKB; PA25403; -.
DR VEuPathDB; HostDB:ENSG00000101425; -.
DR eggNOG; KOG4160; Eukaryota.
DR GeneTree; ENSGT01020000230353; -.
DR HOGENOM; CLU_028970_3_2_1; -.
DR InParanoid; P17213; -.
DR OrthoDB; 1242894at2759; -.
DR PhylomeDB; P17213; -.
DR TreeFam; TF315617; -.
DR PathwayCommons; P17213; -.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR SignaLink; P17213; -.
DR SIGNOR; P17213; -.
DR BioGRID-ORCS; 671; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; BPI; human.
DR EvolutionaryTrace; P17213; -.
DR GenomeRNAi; 671; -.
DR Pharos; P17213; Tbio.
DR PRO; PR:P17213; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P17213; protein.
DR Bgee; ENSG00000101425; Expressed in trabecular bone tissue and 110 other tissues.
DR ExpressionAtlas; P17213; baseline and differential.
DR Genevisible; P17213; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:BHF-UCL.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IDA:BHF-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR InterPro; IPR017943; Bactericidal_perm-incr_a/b_dom.
DR InterPro; IPR030181; BPI.
DR InterPro; IPR030675; BPI/LBP.
DR InterPro; IPR032942; BPI/LBP/Plunc.
DR InterPro; IPR001124; Lipid-bd_serum_glycop_C.
DR InterPro; IPR017954; Lipid-bd_serum_glycop_CS.
DR InterPro; IPR017942; Lipid-bd_serum_glycop_N.
DR PANTHER; PTHR10504; PTHR10504; 1.
DR PANTHER; PTHR10504:SF84; PTHR10504:SF84; 1.
DR Pfam; PF01273; LBP_BPI_CETP; 1.
DR Pfam; PF02886; LBP_BPI_CETP_C; 1.
DR PIRSF; PIRSF002417; Lipid_binding_protein; 1.
DR SMART; SM00328; BPI1; 1.
DR SMART; SM00329; BPI2; 1.
DR SUPFAM; SSF55394; SSF55394; 2.
DR PROSITE; PS00400; LBP_BPI_CETP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:1937776,
FT ECO:0000269|PubMed:2501794, ECO:0000269|PubMed:2722846,
FT ECO:0000269|PubMed:3667613"
FT CHAIN 32..487
FT /note="Bactericidal permeability-increasing protein"
FT /id="PRO_0000017154"
FT REGION 32..42
FT /note="Central sheet, part 1"
FT /evidence="ECO:0000269|PubMed:10843855"
FT REGION 41..224
FT /note="N-terminal barrel"
FT /evidence="ECO:0000269|PubMed:10843855"
FT REGION 226..290
FT /note="Central sheet, part 2"
FT /evidence="ECO:0000269|PubMed:10843855"
FT REGION 240..245
FT /note="Cleavage sites for elastase"
FT /evidence="ECO:0000255"
FT REGION 291..461
FT /note="C-terminal barrel"
FT /evidence="ECO:0000269|PubMed:10843855"
FT REGION 468..487
FT /note="Central sheet, part 3"
FT /evidence="ECO:0000269|PubMed:10843855"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 166..206
FT /evidence="ECO:0000269|PubMed:10843855"
FT VARIANT 12
FT /note="A -> T (in dbSNP:rs5743497)"
FT /id="VAR_049728"
FT VARIANT 12
FT /note="A -> V (in dbSNP:rs5743498)"
FT /id="VAR_049729"
FT VARIANT 16
FT /note="A -> V (in dbSNP:rs1341023)"
FT /evidence="ECO:0000269|PubMed:2722846, ECO:0000269|Ref.3"
FT /id="VAR_018401"
FT VARIANT 90
FT /note="R -> C (in dbSNP:rs5743500)"
FT /id="VAR_049730"
FT VARIANT 140
FT /note="E -> Q (in dbSNP:rs5743506)"
FT /id="VAR_049732"
FT VARIANT 196
FT /note="A -> V (in dbSNP:rs5743509)"
FT /id="VAR_018402"
FT VARIANT 216
FT /note="E -> K (in dbSNP:rs4358188)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2722846, ECO:0000269|Ref.7"
FT /id="VAR_018403"
FT VARIANT 280
FT /note="A -> V (in dbSNP:rs5741804)"
FT /id="VAR_049733"
FT VARIANT 377
FT /note="V -> I (in dbSNP:rs5743524)"
FT /id="VAR_049734"
FT VARIANT 404
FT /note="N -> D (in dbSNP:rs5741809)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.7"
FT /id="VAR_049735"
FT VARIANT 451
FT /note="K -> E (in dbSNP:rs5743542)"
FT /id="VAR_049736"
FT MUTAGEN 49
FT /note="S->C: No impairment of secretion and increased
FT propensity for dimer formation."
FT /evidence="ECO:0000269|PubMed:8812832"
FT MUTAGEN 163
FT /note="C->A: No impairment of secretion and/or biological
FT activity. Loss of dimer formation."
FT /evidence="ECO:0000269|PubMed:8812832"
FT MUTAGEN 166
FT /note="C->S: Poorly secreted. Loss of LPS-binding and
FT biological activity."
FT /evidence="ECO:0000269|PubMed:8812832"
FT MUTAGEN 206
FT /note="C->A: Not secreted."
FT /evidence="ECO:0000269|PubMed:8812832"
FT CONFLICT 5
FT /note="M -> L (in Ref. 6; AAH40955)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="T -> R (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="P -> S (in Ref. 7; AAG42844)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="F -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="K -> R (in Ref. 7; AAG42844)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="Q -> L (in Ref. 4; BAG37729)"
FT /evidence="ECO:0000305"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 42..60
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 81..93
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1EWF"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 106..126
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 129..153
FT /evidence="ECO:0007829|PDB:1EWF"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 194..215
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 383..392
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 416..424
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 433..443
FT /evidence="ECO:0007829|PDB:1EWF"
FT HELIX 445..454
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 464..474
FT /evidence="ECO:0007829|PDB:1EWF"
FT STRAND 477..486
FT /evidence="ECO:0007829|PDB:1EWF"
SQ SEQUENCE 487 AA; 53900 MW; 30BC73B1B465B62D CRC64;
MRENMARGPC NAPRWASLMV LVAIGTAVTA AVNPGVVVRI SQKGLDYASQ QGTAALQKEL
KRIKIPDYSD SFKIKHLGKG HYSFYSMDIR EFQLPSSQIS MVPNVGLKFS ISNANIKISG
KWKAQKRFLK MSGNFDLSIE GMSISADLKL GSNPTSGKPT ITCSSCSSHI NSVHVHISKS
KVGWLIQLFH KKIESALRNK MNSQVCEKVT NSVSSELQPY FQTLPVMTKI DSVAGINYGL
VAPPATTAET LDVQMKGEFY SENHHNPPPF APPVMEFPAA HDRMVYLGLS DYFFNTAGLV
YQEAGVLKMT LRDDMIPKES KFRLTTKFFG TFLPEVAKKF PNMKIQIHVS ASTPPHLSVQ
PTGLTFYPAV DVQAFAVLPN SSLASLFLIG MHTTGSMEVS AESNRLVGEL KLDRLLLELK
HSNIGPFPVE LLQDIMNYIV PILVLPRVNE KLQKGFPLPT PARVQLYNVV LQPHQNFLLF
GADVVYK
